+検索条件
-Structure paper
タイトル | Structural basis of GABA receptor-G protein coupling. |
---|---|
ジャーナル・号・ページ | Nature, Vol. 594, Issue 7864, Page 594-598, Year 2021 |
掲載日 | 2021年4月28日 |
著者 | Cangsong Shen / Chunyou Mao / Chanjuan Xu / Nan Jin / Huibing Zhang / Dan-Dan Shen / Qingya Shen / Xiaomei Wang / Tingjun Hou / Zhong Chen / Philippe Rondard / Jean-Philippe Pin / Yan Zhang / Jianfeng Liu / |
PubMed 要旨 | G-protein-coupled receptors (GPCRs) have central roles in intercellular communication. Structural studies have revealed how GPCRs can activate G proteins. However, whether this mechanism is ...G-protein-coupled receptors (GPCRs) have central roles in intercellular communication. Structural studies have revealed how GPCRs can activate G proteins. However, whether this mechanism is conserved among all classes of GPCR remains unknown. Here we report the structure of the class-C heterodimeric GABA receptor, which is activated by the inhibitory transmitter GABA, in its active form complexed with G protein. We found that a single G protein interacts with the GB2 subunit of the GABA receptor at a site that mainly involves intracellular loop 2 on the side of the transmembrane domain. This is in contrast to the G protein binding in a central cavity, as has been observed with other classes of GPCR. This binding mode results from the active form of the transmembrane domain of this GABA receptor being different from that of other GPCRs, as it shows no outside movement of transmembrane helix 6. Our work also provides details of the inter- and intra-subunit changes that link agonist binding to G-protein activation in this heterodimeric complex. |
リンク | Nature / PubMed:33911284 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.5 Å |
構造データ | EMDB-31049, PDB-7eb2: |
化合物 | ChemComp-2C0: ChemComp-FN0: |
由来 |
|
キーワード | MEMBRANE PROTEIN / GABAB / Cryo-EM / GPCR / Gi |